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Dissociation of protein kinase c activation and sn 1 2 diacylglycerol formation comparison of phosphatidylinositol and phosphatidylcholine derived diglycerides in alpha thrombin stimulated fibroblasts



Dissociation of protein kinase c activation and sn 1 2 diacylglycerol formation comparison of phosphatidylinositol and phosphatidylcholine derived diglycerides in alpha thrombin stimulated fibroblasts



Journal of Cellular Biochemistry Supplement (15 PART B): 159



Diacylglycerols (DAGs) derived from phosphatidylcholine (PC) hydrolysis have been shown to activate protein kinase C (PKC) in vitro, but it is not known whether this event occurs in response to DAGs generated via agonist-induced PC hydrolysis in intact cells. In this report we have addressed this question directly, using .alpha.-thrombin stimulation of IIC9 fibroblasts. PKC activation in intact cells was assessed in two ways, by measuring: 1) PKC membrane association as determined by kinase activity and Western blot analysis and 2) the phosphorylation of an endogenous PKC substrate, an 80-kDa protein. Treatment with 500 ng/ml .alpha.-thrombin has been shown to stimulate both phosphoinositide and PC hydrolysis, whereas treatment with 100 pg/ml .alpha.-thrombin stimulates only PKC breakdown. Using these two conditions, we show that DAG produced from phosphoinositide, but not PC hydrolysis, is associated with the activation of PKC.

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Accession: 007218306

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PMID: 1993695



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